ABLM1_MOUSE
ID ABLM1_MOUSE Reviewed; 861 AA.
AC Q8K4G5; Q80U86; Q8BIR9; Q8K4G3; Q8K4G4;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Actin-binding LIM protein 1;
DE Short=abLIM-1;
DE AltName: Full=Actin-binding LIM protein family member 1;
GN Name=Ablim1; Synonyms=Ablim, Kiaa0059;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RC STRAIN=C57BL/6J;
RX PubMed=9245787; DOI=10.1083/jcb.138.3.575;
RA Roof D.J., Hayes A., Adamian M., Chishti A.H., Li T.;
RT "Molecular characterization of abLIM, a novel actin-binding and double zinc
RT finger protein.";
RL J. Cell Biol. 138:575-588(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11163266; DOI=10.1016/s0896-6273(00)00153-7;
RA Erkman L., Yates P.A., McLaughlin T., McEvilly R.J., Whisenhunt T.,
RA O'Connell S.M., Krones A.I., Kirby M.A., Rapaport D.H.,
RA Bermingham J.R. Jr., O'Leary D.D.M., Rosenfeld M.G.;
RT "A POU domain transcription factor-dependent program regulates axon
RT pathfinding in the vertebrate visual system.";
RL Neuron 28:779-792(2000).
RN [5]
RP FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING
RP (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J;
RX PubMed=12849746; DOI=10.1016/s0306-4522(03)00263-x;
RA Lu C., Huang X., Ma H.F., Gooley J.J., Aparacio J., Roof D.J., Chen C.,
RA Chen D.F., Li T.;
RT "Normal retinal development and retinofugal projections in mice lacking the
RT retina-specific variant of actin-binding LIM domain protein.";
RL Neuroscience 120:121-131(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411 AND SER-499, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-440, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-411; SER-466;
RP SER-470; SER-475; SER-479; SER-499; SER-502; SER-582; SER-671 AND SER-760,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May act as scaffold protein (By similarity). May play a role
CC in the development of the retina. Has been suggested to play a role in
CC axon guidance. {ECO:0000250, ECO:0000269|PubMed:11163266,
CC ECO:0000269|PubMed:12849746}.
CC -!- SUBUNIT: Binds F-actin. Interacts with ABRA (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q8K4G5; Q62108: Dlg4; NbExp=5; IntAct=EBI-2307994, EBI-300895;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9245787}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9245787}. Note=In a striped
CC pattern along the myofibril axis in cardiac myocytes. Associated with
CC the cytoskeleton.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=AbLIM-L;
CC IsoId=Q8K4G5-1; Sequence=Displayed;
CC Name=2; Synonyms=AbLIM-M;
CC IsoId=Q8K4G5-2; Sequence=VSP_012104, VSP_012108, VSP_012110;
CC Name=3; Synonyms=AbLIM-S;
CC IsoId=Q8K4G5-3; Sequence=VSP_012103;
CC Name=4;
CC IsoId=Q8K4G5-4; Sequence=VSP_012104, VSP_012108, VSP_012110,
CC VSP_012111;
CC Name=5;
CC IsoId=Q8K4G5-5; Sequence=VSP_012105, VSP_012106, VSP_012107,
CC VSP_012109;
CC -!- TISSUE SPECIFICITY: Isoform 1 is detected in adult retina, where it is
CC highly expressed in the ganglion layer. Detected in rod inner segment.
CC Isoform 2 is highly expressed in adult retina, brain, kidney and heart.
CC Isoform 3 is highly expressed in adult retina, brain, kidney, liver,
CC skeletal muscle, spleen and heart. Detected in embryonic retina, brain,
CC spinal cord, peripheral sensory ganglia and thymus.
CC {ECO:0000269|PubMed:11163266, ECO:0000269|PubMed:12849746,
CC ECO:0000269|PubMed:9245787}.
CC -!- DEVELOPMENTAL STAGE: Isoform 1 is detected at low levels starting from
CC 12 dpc and remains constant until birth. After this levels increase
CC strongly and expression remains high in adults. Isoform 2 and isoform 3
CC are expressed at a constant high level throughout development.
CC {ECO:0000269|PubMed:12849746, ECO:0000269|PubMed:9245787}.
CC -!- MISCELLANEOUS: Isoform 1 is not necessary for normal axon guidance.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65478.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF404774; AAM73705.1; -; mRNA.
DR EMBL; AF404775; AAM73706.1; -; mRNA.
DR EMBL; AF404776; AAM73707.1; -; mRNA.
DR EMBL; AK122196; BAC65478.1; ALT_INIT; mRNA.
DR EMBL; AK029371; BAC26424.1; -; mRNA.
DR CCDS; CCDS38027.1; -. [Q8K4G5-1]
DR CCDS; CCDS50478.1; -. [Q8K4G5-3]
DR CCDS; CCDS50479.1; -. [Q8K4G5-2]
DR CCDS; CCDS70964.1; -. [Q8K4G5-4]
DR RefSeq; NP_001096647.1; NM_001103177.2. [Q8K4G5-2]
DR RefSeq; NP_001096648.1; NM_001103178.2.
DR RefSeq; NP_001277742.1; NM_001290813.1.
DR RefSeq; NP_001277744.1; NM_001290815.1. [Q8K4G5-4]
DR RefSeq; NP_848803.3; NM_178688.3.
DR AlphaFoldDB; Q8K4G5; -.
DR SMR; Q8K4G5; -.
DR BioGRID; 230492; 12.
DR IntAct; Q8K4G5; 6.
DR MINT; Q8K4G5; -.
DR STRING; 10090.ENSMUSP00000078336; -.
DR iPTMnet; Q8K4G5; -.
DR PhosphoSitePlus; Q8K4G5; -.
DR EPD; Q8K4G5; -.
DR jPOST; Q8K4G5; -.
DR MaxQB; Q8K4G5; -.
DR PaxDb; Q8K4G5; -.
DR PeptideAtlas; Q8K4G5; -.
DR PRIDE; Q8K4G5; -.
DR ProteomicsDB; 285909; -. [Q8K4G5-1]
DR ProteomicsDB; 285910; -. [Q8K4G5-2]
DR ProteomicsDB; 285911; -. [Q8K4G5-3]
DR ProteomicsDB; 285912; -. [Q8K4G5-4]
DR ProteomicsDB; 285913; -. [Q8K4G5-5]
DR Antibodypedia; 31944; 197 antibodies from 28 providers.
DR DNASU; 226251; -.
DR Ensembl; ENSMUST00000099294; ENSMUSP00000096897; ENSMUSG00000025085. [Q8K4G5-4]
DR Ensembl; ENSMUST00000111524; ENSMUSP00000107149; ENSMUSG00000025085. [Q8K4G5-5]
DR Ensembl; ENSMUST00000111546; ENSMUSP00000107172; ENSMUSG00000025085. [Q8K4G5-2]
DR GeneID; 226251; -.
DR KEGG; mmu:226251; -.
DR UCSC; uc008hzz.1; mouse. [Q8K4G5-5]
DR UCSC; uc033hkz.2; mouse. [Q8K4G5-2]
DR UCSC; uc033hld.2; mouse. [Q8K4G5-4]
DR CTD; 3983; -.
DR MGI; MGI:1194500; Ablim1.
DR VEuPathDB; HostDB:ENSMUSG00000025085; -.
DR eggNOG; KOG1044; Eukaryota.
DR GeneTree; ENSGT00950000182850; -.
DR HOGENOM; CLU_001357_12_3_1; -.
DR InParanoid; Q8K4G5; -.
DR OMA; VENRHFH; -.
DR OrthoDB; 192350at2759; -.
DR PhylomeDB; Q8K4G5; -.
DR BioGRID-ORCS; 226251; 1 hit in 58 CRISPR screens.
DR ChiTaRS; Ablim1; mouse.
DR PRO; PR:Q8K4G5; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8K4G5; protein.
DR Bgee; ENSMUSG00000025085; Expressed in cardiac muscle of left ventricle and 269 other tissues.
DR ExpressionAtlas; Q8K4G5; baseline and differential.
DR Genevisible; Q8K4G5; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR GO; GO:0001725; C:stress fiber; ISO:MGI.
DR GO; GO:0003779; F:actin binding; IDA:MGI.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007411; P:axon guidance; IDA:MGI.
DR GO; GO:0060271; P:cilium assembly; ISO:MGI.
DR GO; GO:0007010; P:cytoskeleton organization; IEA:InterPro.
DR GO; GO:0030032; P:lamellipodium assembly; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:MGI.
DR Gene3D; 1.10.950.10; -; 1.
DR InterPro; IPR028448; ABLIM1.
DR InterPro; IPR032402; AbLIM_anchor.
DR InterPro; IPR003128; Villin_headpiece.
DR InterPro; IPR036886; Villin_headpiece_dom_sf.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24213:SF18; PTHR24213:SF18; 1.
DR Pfam; PF16182; AbLIM_anchor; 1.
DR Pfam; PF00412; LIM; 4.
DR Pfam; PF02209; VHP; 1.
DR SMART; SM00132; LIM; 4.
DR SMART; SM00153; VHP; 1.
DR SUPFAM; SSF47050; SSF47050; 1.
DR PROSITE; PS51089; HP; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 4.
DR PROSITE; PS50023; LIM_DOMAIN_2; 4.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Isopeptide bond; LIM domain; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation; Zinc.
FT CHAIN 1..861
FT /note="Actin-binding LIM protein 1"
FT /id="PRO_0000075698"
FT DOMAIN 97..156
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 156..216
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 224..283
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 283..343
FT /note="LIM zinc-binding 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 793..861
FT /note="HP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00595"
FT REGION 374..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 673..723
FT /evidence="ECO:0000255"
FT COMPBIAS 377..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..682
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 417
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O14639"
FT MOD_RES 440
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 477
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O14639"
FT MOD_RES 479
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 483
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O14639"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14639"
FT MOD_RES 499
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 671
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 723
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14639"
FT MOD_RES 738
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14639"
FT MOD_RES 760
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 789
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14639"
FT CROSSLNK 704
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O14639"
FT VAR_SEQ 1..316
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9245787"
FT /id="VSP_012103"
FT VAR_SEQ 1..81
FT /note="MPSLLGLKCLGKLCSSEIGKVPSPERASLRNSHRRLLIEDLSVPETPDPAHR
FT RRGTVIHLVYLYSAGCGPPELRFSSYDPS -> MVKEK (in isoform 2 and
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:12693553,
FT ECO:0000303|PubMed:9245787"
FT /id="VSP_012104"
FT VAR_SEQ 1..77
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012105"
FT VAR_SEQ 78..81
FT /note="YDPS -> MSTR (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012106"
FT VAR_SEQ 301..345
FT /note="DKHYHPSCARCSRCNQMFTEGEEMYLQGSTVWHPDCKQSTKTEEK -> VTE
FT ASRTWSHIDLRWQGRSEELRAWRHSIQSLRHQSAREWFALSA (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012107"
FT VAR_SEQ 346..861
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012109"
FT VAR_SEQ 348..391
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12693553,
FT ECO:0000303|PubMed:9245787"
FT /id="VSP_012108"
FT VAR_SEQ 525..564
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12693553,
FT ECO:0000303|PubMed:9245787"
FT /id="VSP_012110"
FT VAR_SEQ 616..662
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_012111"
SQ SEQUENCE 861 AA; 96805 MW; 5E045F7CEF1D91EF CRC64;
MPSLLGLKCL GKLCSSEIGK VPSPERASLR NSHRRLLIED LSVPETPDPA HRRRGTVIHL
VYLYSAGCGP PELRFSSYDP SVAHPQDPHH SSEKPVIHCH KCGEPCKGEV LRVQTKHFHI
KCFTCKVCGC DLAQGGFFIK NGDYLCTLDY QRMYGTRCHG CGEFVEGEVV TALGKTYHPN
CFACTICKRP FPPGDRVTFN GRDCLCQLCA QPMSSSPKEA SCSSNCAGCG RDIKNGQALL
ALDKQWHLGC FKCKSCGKVL TGEYISKDGS PYCEKDYQGL FGVKCEACHQ FITGKVLEAG
DKHYHPSCAR CSRCNQMFTE GEEMYLQGST VWHPDCKQST KTEEKLRPPN IPRSSSDFFY
PKSLIRRTGR SPALQLLSPP CLTNSNKNPR QPTRTSSESI YSRPGSSIPG SPGHTIYAKV
DNEILDYKDL AAIPKVKAIY DIERPDLITY EPFYTSGYED KQERQSLGES PRTLSPTPSA
EGYQDVRDRM IHRSTSQGSI NSPVYSRHSY TPTTSRSPQH FHRPELLSPG VHRWSPLRTS
SFSSTHSDSR PNPPFRHHFL PHVKGNEPSS GRNSPLPYRP DSRPLTPTYA QAPKHFHVPD
QGINIYRKPP IYKQHAALAA QSKASEDIIK FSKFPAAQAP DPNEIPKIET DHWPGPPSLA
AVGTDPRRRS SGREEDEEEL LRRRQLQEEQ LMKLNSGLGQ LILKEEMEKE SRERASLASR
YDSPLHSASH APSSKTSSLP GYGKNGLHRP VSTDFAQYNS YGDISGGVRD YQTLPDGHMP
AVRMDRGVSM PNMLEPKIFP YEMLMVTNRG RNKILRDVDR TRLERHLAPE VFWEIFGMSI
QEFDKLPLWR RNDMKKKAKL F
